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- W1970066150 abstract "The negative regulation of the biotin biosynthetic (bio) operon in Escherichia coli is mediated by the bifunctional birA gene product, which serves as the bio repressor and biotin-activating enzyme. Nucleotide sequence analysis of 18 mutations in the birA gene was employed to study the DNA-binding and enzymatic functions of the BirA protein. The results indicate that a predicted helix-turn-helix structure, from amino acid (aa) positions 18 to 39 within the 321-aa BirA protein, may be responsible for sequence-specific DNA binding, whereas the temperature-sensitive mutations affecting biotin activation are found in two regions from aa positions 83-119 and 189-235." @default.
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- W1970066150 date "1986-01-01" @default.
- W1970066150 modified "2023-09-25" @default.
- W1970066150 title "DNA-binding and enzymatic domains of the bifunctional biotin operon repressor (BirA) of Escherichia" @default.
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- W1970066150 doi "https://doi.org/10.1016/0378-1119(86)90189-7" @default.
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